TYY2_HUMAN - dbPTM
TYY2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TYY2_HUMAN
UniProt AC O15391
Protein Name Transcription factor YY2
Gene Name YY2
Organism Homo sapiens (Human).
Sequence Length 372
Subcellular Localization Nucleus .
Protein Description Functions as a multifunctional transcription factor that may exhibit positive and negative control on a large number of genes. May antagonize YY1 and function in development and differentiation..
Protein Sequence MASNEDFSITQDLEIPADIVELHDINVEPLPMEDIPTESVQYEDVDGNWIYGGHNHPPLMVLQPLFTNTGYGDHDQEMLMLQTQEEVVGYCDSDNQLGNDLEDQLALPDSIEDEHFQMTLASLSASAASTSTSTQSRSKKPSKKPSGKSATSTEANPAGSSSSLGTRKWEQKQMQVKTLEGEFSVTMWSPNDNNDQGAVGEGQAENPPDYSEYLKGKKLPPGGLPGIDLSDPKQLAEFTKVKPKRSKGEPPKTVPCSYSGCEKMFRDYAAMRKHLHIHGPRVHVCAECGKAFLESSKLRRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHLRIHTGDKPFVCPFDVCNRKFAQSTNLKTHILTHVKTKNNP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
130PhosphorylationLSASAASTSTSTQSR
HHHHHHCCCCCCCCC
31.15-
144AcetylationRSKKPSKKPSGKSAT
CCCCCCCCCCCCCCC
49.0719825497
148AcetylationPSKKPSGKSATSTEA
CCCCCCCCCCCCCCC
41.0519825503
152PhosphorylationPSGKSATSTEANPAG
CCCCCCCCCCCCCCC
24.78-
160PhosphorylationTEANPAGSSSSLGTR
CCCCCCCCCCCCCCH
29.20-
161PhosphorylationEANPAGSSSSLGTRK
CCCCCCCCCCCCCHH
24.03-
163PhosphorylationNPAGSSSSLGTRKWE
CCCCCCCCCCCHHHE
32.53-
218SumoylationSEYLKGKKLPPGGLP
HHHHCCCCCCCCCCC
74.93-
218UbiquitinationSEYLKGKKLPPGGLP
HHHHCCCCCCCCCCC
74.93-
218SumoylationSEYLKGKKLPPGGLP
HHHHCCCCCCCCCCC
74.93-
233UbiquitinationGIDLSDPKQLAEFTK
CCCCCCHHHHHHHHC
64.0322817900
306PhosphorylationRRHQLVHTGEKPFQC
CCCCCCCCCCCCEEE
39.2925159151
309AcetylationQLVHTGEKPFQCTFE
CCCCCCCCCEEEEEC
53.1023954790
309SumoylationQLVHTGEKPFQCTFE
CCCCCCCCCEEEEEC
53.10-
309UbiquitinationQLVHTGEKPFQCTFE
CCCCCCCCCEEEEEC
53.10-
309SumoylationQLVHTGEKPFQCTFE
CCCCCCCCCEEEEEC
53.10-
314PhosphorylationGEKPFQCTFEGCGKR
CCCCEEEEECCCCCE
17.5924732914
320MethylationCTFEGCGKRFSLDFN
EEECCCCCEEEEEEE
55.11-
323PhosphorylationEGCGKRFSLDFNLRT
CCCCCEEEEEEECCE
30.9428450419
330PhosphorylationSLDFNLRTHLRIHTG
EEEEECCEEEEEECC
28.5526074081
351SumoylationPFDVCNRKFAQSTNL
CHHHCCCHHHHCCCC
30.93-
351UbiquitinationPFDVCNRKFAQSTNL
CHHHCCCHHHHCCCC
30.9329967540
351SumoylationPFDVCNRKFAQSTNL
CHHHCCCHHHHCCCC
30.93-
351AcetylationPFDVCNRKFAQSTNL
CHHHCCCHHHHCCCC
30.9325953088

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TYY2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TYY2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TYY2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RING1_HUMANRING1physical
21530438
RING2_HUMANRNF2physical
21530438

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TYY2_HUMAN

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Related Literatures of Post-Translational Modification

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